Isolation and Characterization of Lectin from the Scallop Patinopecten yessoensis

Chikalovets, I. V.; Mizgina, Tatyana O.; Molchanova, V. I.; Ovcharenko, Yu. S.; Chernikov, Oleg V.

doi:10.1007/s10600-017-2098-9

Cited by 5 publications

(2 citation statements)

References 20 publications

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“…For bivalves lectins such pH stability of hemagglutination activity is not typical. For example, the galactose-specific lectin from the scallop Patinopecten yessoensis is completely inactivated at pH 4.0 and 11.0 [34].…”

Section: Hemagglutinating Activity and The Carbohydrate Specificitymentioning

confidence: 99%

New l-Rhamnose-Binding Lectin from the Bivalve Glycymeris yessoensis: Purification, Partial Structural Characterization and Antibacterial Activity

Mizgina,

Chikalovets,

Bulanova

et al. 2023

Marine Drugs

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In this study, a new l-rhamnose-binding lectin (GYL-R) from the hemolymph of bivalve Glycymeris yessoensis was purified using affinity and ion-exchange chromatography and functionally characterized. Lectin antimicrobial activity was examined in different ways. The lectin was inhibited by saccharides possessing the same configuration of hydroxyl groups at C-2 and C-4, such as l-rhamnose, d-galactose, lactose, l-arabinose and raffinose. Using the glycan microarray approach, natural carbohydrate ligands were established for GYL-R as l-Rha and glycans containing the α-Gal residue in the terminal position. The GYL-R molecular mass determined by MALDI-TOF mass spectrometry was 30,415 Da. The hemagglutination activity of the lectin was not affected by metal ions. The lectin was stable up to 75 °C and between pH 4.0 and 12.0. The amino acid sequence of the five GYL-R segments was obtained with nano-ESI MS/MS and contained both YGR and DPC-peptide motifs which are conserved in most of the l-rhamnose-binding lectin carbohydrate recognition domains. Circular dichroism confirmed that GYL is a α/β-protein with a predominance of the random coil. Furthermore, GYL-R was able to bind and suppress the growth of the Gram-negative bacteria E. coli by recognizing lipopolysaccharides. Together, these results suggest that GYL-R is a new member of the RBL family which participates in the self-defense mechanism against bacteria and pathogens with a distinct carbohydrate-binding specificity.

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Section: Hemagglutinating Activity and The Carbohydrate Specificitymentioning

confidence: 99%

New l-Rhamnose-Binding Lectin from the Bivalve Glycymeris yessoensis: Purification, Partial Structural Characterization and Antibacterial Activity

Mizgina,

Chikalovets,

Bulanova

et al. 2023

Marine Drugs

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“…Today a large number of galactosyl-binding lectins have been reported to occur in the invertebrates, which bind to D-galactose, its derivatives, and D-galactose containing complex carbohydrates in a very selective manner [9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

et al. 2019

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A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.

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First Report on Isolation of N-Isopropyl Palmitamide from the Natural Source Microstylis muscifera: a Potential Chemical Marker for Identification

et al. 2019

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Isolation and Characterization of Lectin from the Scallop Patinopecten yessoensis

Cited by 5 publications

References 20 publications

New l-Rhamnose-Binding Lectin from the Bivalve Glycymeris yessoensis: Purification, Partial Structural Characterization and Antibacterial Activity

New l-Rhamnose-Binding Lectin from the Bivalve Glycymeris yessoensis: Purification, Partial Structural Characterization and Antibacterial Activity

Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

First Report on Isolation of N-Isopropyl Palmitamide from the Natural Source Microstylis muscifera: a Potential Chemical Marker for Identification

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